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• W2889094087 abstract "The free sulphydryl groups in factor Va were analyzed under native and denaturing conditions using dithio-bis-nitrobenzoic acid (DTNB). The heavy chain (D) and the light chain (E) of factor Va were found to contain one free sulphydryl each under native conditions and following denaturation. Intact factor Va contained two free sulphydryls after denaturation while only one of these groups was accessible to DTNB under native conditions. Analysis of the rates of modification of the accessible sulphydryl in factor Va, and direct visualization of factor Va reacted with fluorescent sulphydryl modifiers and analyzed by SDS-PAGE, indicated that the accessible group was present in component D. Factor Va was labelled with the sulphydryl-directed flurophore N-pyrene-l-malemide with no loss in functional activity. Fluorescently modified Va (PYR-Va) contained between 0.83 and 0.91 moles pyrene and showed a concomittant loss in the free sulphydryls accessible to DTNB. Fluorescence polarization studies indicated that the binding of PYR-Va to phospholipid vessicles composed of phosphatidylcholine (PC) and phosphatidylserine (PS) was accompanied by a significant increase in the fluorescence polarization of the pyrene moiety. Systematic analysis of the binding of PYR-Va to PCPS (75%PC, 25%PS) indicated that the binding interaction was characterized by a Kd=2.7x10−9 M and a stoichiometry of 42 monomeric phospholipids per lipid combining site. The binding of PYR-Va to PCPS was independent of added calcium ion and could be reversed by the addition of unlabelled factor Va. Analysis of the displacement curves indicated that native factor Va and PYR-Va mutually excluded each other with identical affinities (Kd=2.5×10−9 M). Isolated component D had no effect on the interaction between PYR-Va and PCPS, while isolated component E was capable of disrupting the PYR-Va-PCPS interaction (Kd=3.1×10−9 M%) indicating that this subunit entirely mediates the interaction between Va and PCPS. No detectable binding of PYR-Va was observed when 100% PC vesicles were used and systematic variation of the PS content of the vesicles indicated that this parameter linearly influenced the stoichiometry of the PYR-Va-PCPS interaction with a minimal effect on the dissociation constant for the reaction. The data indicate that the factor Va-binding site is determined by the PS content of the lipid bilayer. (Supported by NIH grants HL-35058 and HL-34575)" @default.
• W2889094087 created "2018-09-07" @default.
• W2889094087 creator A5036209779 @default.
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• W2889094087 date "1987-01-01" @default.
• W2889094087 modified "2023-09-23" @default.
• W2889094087 title "FLUORESCENCE STUDIES OF THE BINDING OF FACTOR Va TO PHOSPHOLIPID VESICLES" @default.
• W2889094087 doi "https://doi.org/10.1055/s-0038-1643882" @default.
• W2889094087 hasPublicationYear "1987" @default.
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